Endo-1,4-beta-xylanase A
Details
- Name
- Endo-1,4-beta-xylanase A
- Synonyms
- 1,4-beta-D-xylan xylanohydrolase A
- 3.2.1.8
- Xylanase A
- Gene Name
- xlnA
- Organism
- Streptomyces lividans
- Amino acid sequence
>lcl|BSEQ0019328|Endo-1,4-beta-xylanase A MGSYALPRSGVRRSIRVLLLALVVGVLGTATALIAPPGAHAAESTLGAAAAQSGRYFGTA IASGRLSDSTYTSIAGREFNMVTAENEMKIDATEPQRGQFNFSSADRVYNWAVQNGKQVR GHTLAWHSQQPGWMQSLSGSALRQAMIDHINGVMAHYKGKIVQWDVVNEAFADGSSGARR DSNLQRSGNDWIEVAFRTARAADPSAKLCYNDYNVENWTWAKTQAMYNMVRDFKQRGVPI DCVGFQSHFNSGSPYNSNFRTTLQNFAALGVDVAITELDIQGAPASTYANVTNDCLAVSR CLGITVWGVRDSDSWRSEQTPLLFNNDGSKKAAYTAVLDALNGGDSSEPPADGGQIKGVG SGRCLDVPDASTSDGTQLQLWDCHSGTNQQWAATDAGELRVYGDKCLDAAGTSNGSKVQI YSCWGGDNQKWRLNSDGSVVGVQSGLCLDAVGNGTANGTLIQLYTCSNGSNQRWTRT
- Number of residues
- 477
- Molecular Weight
- 51162.3
- Theoretical pI
- 6.61
- GO Classification
- Functionscarbohydrate binding / endo-1,4-beta-xylanase activityProcessesxylan catabolic processComponentsextracellular region
- General Function
- Endo-1,4-beta-xylanase activity
- Specific Function
- Contributes to hydrolyze hemicellulose, the major component of plant cell-walls. XLNA and XLNB seem to act sequentially on the substrate to yield xylobiose and xylose as carbon sources.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Secreted
- Gene sequence
>lcl|BSEQ0005418|1434 bp ATGGGCTCCTACGCCCTTCCCAGATCAGGTGTCCGCAGGAGCATTCGCGTCCTGCTGCTG GCGCTGGTCGTCGGCGTACTCGGCACGGCCACCGCACTGATCGCGCCGCCGGGGGCACAC GCCGCCGAGAGCACGCTCGGCGCCGCGGCGGCGCAGAGCGGCCGCTACTTCGGCACCGCC ATCGCCTCGGGCAGGCTGAGCGACTCGACGTACACGTCGATCGCGGGCCGTGAGTTCAAC ATGGTGACGGCCGAGAACGAGATGAAGATCGACGCCACCGAACCGCAGCGGGGCCAGTTC AACTTCAGCTCCGCCGACCGCGTCTACAACTGGGCGGTGCAGAACGGCAAGCAGGTGCGC GGCCACACCCTGGCCTGGCACTCCCAGCAGCCCGGCTGGATGCAGAGCCTCAGCGGCAGC GCGCTGCGCCAGGCGATGATCGACCACATCAACGGCGTGATGGCCCACTACAAGGGCAAG ATCGTCCAGTGGGACGTCGTGAACGAGGCCTTCGCCGACGGCAGTTCGGGAGCGCGGCGG GACTCCAACCTGCAACGCAGCGGCAACGACTGGATCGAGGTCGCCTTCCGCACCGCGCGC GCCGCCGACCCGTCCGCCAAGCTCTGCTACAACGACTACAACGTCGAGAACTGGACCTGG GCCAAGACCCAGGCCATGTACAACATGGTGCGGGACTTCAAGCAGCGCGGCGTGCCGATC GACTGCGTCGGCTTCCAGTCGCACTTCAACAGCGGCAGCCCCTACAACAGCAACTTCCGC ACCACACTGCAGAACTTCGCCGCCCTCGGCGTCGACGTGGCCATCACCGAGCTGGACATC CAGGGCGCCCCGGCCTCGACCTACGCCAACGTGACCAACGACTGCCTGGCCGTCTCGCGC TGCCTCGGCATCACCGTCTGGGGTGTGCGCGACAGCGACTCCTGGCGGTCGGAGCAGACG CCGTTGCTGTTCAACAACGACGGCAGCAAGAAGGCCGCGTACACCGCCGTCCTCGACGCA CTCAACGGCGGCGACTCCTCGGAGCCCCCCGCGGACGGGGGACAGATCAAGGGCGTCGGT TCGGGCCGCTGCCTCGACGTGCCCGACGCCAGCACCTCCGACGGCACCCAGCTCCAGCTG TGGGACTGCCACAGCGGCACCAACCAGCAGTGGGCCGCCACTGACGCGGGCGAGCTCAGG GTCTACGGCGACAAGTGCCTGGACGCCGCAGGCACCAGCAACGGCTCCAAGGTCCAGATC TACAGCTGCTGGGGCGGCGACAACCAGAAGTGGCGCCTCAACTCCGACGGGTCCGTCGTC GGCGTCCAGTCCGGCCTCTGCCTCGACGCCGTCGGGAACGGCACGGCCAACGGCACCCTG ATCCAGCTGTACACCTGCTCCAACGGCAGCAACCAACGCTGGACCCGCACCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P26514 UniProtKB Entry Name XYNA_STRLI GenBank Gene ID M64551 - General References
- Shareck F, Roy C, Yaguchi M, Morosoli R, Kluepfel D: Sequences of three genes specifying xylanases in Streptomyces lividans. Gene. 1991 Oct 30;107(1):75-82. [Article]
- Derewenda U, Swenson L, Green R, Wei Y, Morosoli R, Shareck F, Kluepfel D, Derewenda ZS: Crystal structure, at 2.6-A resolution, of the Streptomyces lividans xylanase A, a member of the F family of beta-1,4-D-glycanases. J Biol Chem. 1994 Aug 19;269(33):20811-4. [Article]
- Notenboom V, Boraston AB, Williams SJ, Kilburn DG, Rose DR: High-resolution crystal structures of the lectin-like xylan binding domain from Streptomyces lividans xylanase 10A with bound substrates reveal a novel mode of xylan binding. Biochemistry. 2002 Apr 2;41(13):4246-54. [Article]